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P25398

- RS12_HUMAN

UniProt

P25398 - RS12_HUMAN

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Protein

40S ribosomal protein S12

Gene

RPS12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  5. RNA metabolic process Source: Reactome
  6. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  7. translation Source: UniProtKB
  8. translational elongation Source: Reactome
  9. translational initiation Source: Reactome
  10. translational termination Source: Reactome
  11. viral life cycle Source: Reactome
  12. viral process Source: Reactome
  13. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S12
Gene namesi
Name:RPS12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:10385. RPS12.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic small ribosomal subunit Source: UniProtKB
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34784.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 13213140S ribosomal protein S12PRO_0000122323Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 Publications
Modified residuei129 – 1291N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP25398.
PaxDbiP25398.
PRIDEiP25398.

2D gel databases

UCD-2DPAGEP25398.

PTM databases

PhosphoSiteiP25398.

Expressioni

Gene expression databases

BgeeiP25398.
CleanExiHS_RPS12.
GenevestigatoriP25398.

Organism-specific databases

HPAiHPA006124.

Interactioni

Protein-protein interaction databases

BioGridi112120. 96 interactions.
IntActiP25398. 12 interactions.
MINTiMINT-1160578.
STRINGi9606.ENSP00000230050.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00M1-132[»]
ProteinModelPortaliP25398.
SMRiP25398. Positions 11-130.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S12e family.Curated

Phylogenomic databases

eggNOGiCOG1358.
GeneTreeiENSGT00390000018318.
HOGENOMiHOG000210688.
HOVERGENiHBG001720.
InParanoidiP25398.
KOiK02951.
OMAiANNCDEP.
OrthoDBiEOG7H1JP3.
PhylomeDBiP25398.
TreeFamiTF300196.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR029064. L30e-like.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR000530. Ribosomal_S12e.
[Graphical view]
PANTHERiPTHR11843. PTHR11843. 1 hit.
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
PRINTSiPR00972. RIBSOMALS12E.
SUPFAMiSSF55315. SSF55315. 1 hit.
PROSITEiPS01189. RIBOSOMAL_S12E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25398-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEEGIAAGG VMDVNTALQE VLKTALIHDG LARGIREAAK ALDKRQAHLC
60 70 80 90 100
VLASNCDEPM YVKLVEALCA EHQINLIKVD DNKKLGEWVG LCKIDREGKP
110 120 130
RKVVGCSCVV VKDYGKESQA KDVIEEYFKC KK
Length:132
Mass (Da):14,515
Last modified:March 3, 2009 - v3
Checksum:i45AD1274D55FFA25
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521L → Q in CAA37582. (PubMed:1861993)Curated
Sequence conflicti69 – 691C → L in CAA37582. (PubMed:1861993)Curated
Sequence conflicti99 – 991K → N in CAA37582. (PubMed:1861993)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53505 mRNA. Translation: CAA37582.1.
AB061840 Genomic DNA. Translation: BAB79478.1.
AK311826 mRNA. Translation: BAG34768.1.
AL137783 Genomic DNA. Translation: CAC12946.1.
CH471051 Genomic DNA. Translation: EAW48011.1.
BC017321 mRNA. Translation: AAH17321.1.
BC071930 mRNA. Translation: AAH71930.1.
BC095424 mRNA. Translation: AAH95424.1.
AB007153 Genomic DNA. Translation: BAA25819.1.
CCDSiCCDS5164.1.
PIRiS22989. R3HU12.
RefSeqiNP_001007.2. NM_001016.3.
UniGeneiHs.546289.

Genome annotation databases

EnsembliENST00000230050; ENSP00000230050; ENSG00000112306.
GeneIDi6206.
KEGGihsa:6206.
UCSCiuc003qdx.3. human.

Polymorphism databases

DMDMi224471878.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53505 mRNA. Translation: CAA37582.1 .
AB061840 Genomic DNA. Translation: BAB79478.1 .
AK311826 mRNA. Translation: BAG34768.1 .
AL137783 Genomic DNA. Translation: CAC12946.1 .
CH471051 Genomic DNA. Translation: EAW48011.1 .
BC017321 mRNA. Translation: AAH17321.1 .
BC071930 mRNA. Translation: AAH71930.1 .
BC095424 mRNA. Translation: AAH95424.1 .
AB007153 Genomic DNA. Translation: BAA25819.1 .
CCDSi CCDS5164.1.
PIRi S22989. R3HU12.
RefSeqi NP_001007.2. NM_001016.3.
UniGenei Hs.546289.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3A electron microscopy 5.00 M 1-132 [» ]
ProteinModelPortali P25398.
SMRi P25398. Positions 11-130.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112120. 96 interactions.
IntActi P25398. 12 interactions.
MINTi MINT-1160578.
STRINGi 9606.ENSP00000230050.

PTM databases

PhosphoSitei P25398.

Polymorphism databases

DMDMi 224471878.

2D gel databases

UCD-2DPAGE P25398.

Proteomic databases

MaxQBi P25398.
PaxDbi P25398.
PRIDEi P25398.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000230050 ; ENSP00000230050 ; ENSG00000112306 .
GeneIDi 6206.
KEGGi hsa:6206.
UCSCi uc003qdx.3. human.

Organism-specific databases

CTDi 6206.
GeneCardsi GC06P133136.
HGNCi HGNC:10385. RPS12.
HPAi HPA006124.
MIMi 603660. gene.
neXtProti NX_P25398.
PharmGKBi PA34784.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1358.
GeneTreei ENSGT00390000018318.
HOGENOMi HOG000210688.
HOVERGENi HBG001720.
InParanoidi P25398.
KOi K02951.
OMAi ANNCDEP.
OrthoDBi EOG7H1JP3.
PhylomeDBi P25398.
TreeFami TF300196.

Enzyme and pathway databases

Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSi RPS12. human.
GeneWikii RPS12.
GenomeRNAii 6206.
NextBioi 24103.
PROi P25398.
SOURCEi Search...

Gene expression databases

Bgeei P25398.
CleanExi HS_RPS12.
Genevestigatori P25398.

Family and domain databases

Gene3Di 3.30.1330.30. 1 hit.
InterProi IPR029064. L30e-like.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR000530. Ribosomal_S12e.
[Graphical view ]
PANTHERi PTHR11843. PTHR11843. 1 hit.
Pfami PF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view ]
PRINTSi PR00972. RIBSOMALS12E.
SUPFAMi SSF55315. SSF55315. 1 hit.
PROSITEi PS01189. RIBOSOMAL_S12E. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA and predicted amino acid sequences of the human ribosomal protein genes rpS12 and rpL17."
    Herault Y., Michel D., Chatelain G., Brun G.
    Nucleic Acids Res. 19:4001-4001(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
    Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
    Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic stem cell and Skin.
  7. Cited for: PROTEIN SEQUENCE OF 2-33; 85-93 AND 117-129, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma, Hepatoma and Mammary carcinoma.
  8. "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
    Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
    Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-39.
    Tissue: Placenta.
  9. "A map of 75 human ribosomal protein genes."
    Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
    Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-125.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRS12_HUMAN
AccessioniPrimary (citable) accession number: P25398
Secondary accession number(s): Q76M58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: March 3, 2009
Last modified: November 26, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3